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Scientific Interest(s):

Research in Dr. Todd Yeates' laboratory addresses problems at the interface of molecular biology, mathematics and computation. Interests cover various aspects of protein structure and function, protein sequence and evolution and protein assembly and design. Yeates and his colleagues are using protein crystallography to explore the structure and function of enzymes whose activities are of special interest, such as adenylosuccinate (implicated in some forms of autism) and protein aspartyl methyltransferase (important in repairing damaged proteins). Computational approaches are being used to attack the long-standing phase problem of macromolecular crystallography, most recently by pattern recognition methods.

In the area of protein evolution, the researchers are taking advantage of the data from the growing number of organisms whose genomes have been completely sequenced to investigate unusual mechanisms of protein evolution, and to develop new approaches to the problem of predicting the cellular roles of proteins from their amino acid sequences. Finally, building on the lab's continuing interest in the symmetry of protein assemblies, the researchers have developed a new and general strategy for designing novel proteins that self-assemble into a variety of regular structures or material, including cages, filaments, layers and crystals. They call this new class of designed structures "nanohedra," to suggest their scale and symmetry.